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c. ruiz, f.i.j. pastor and p. diaz. 2005.To isolate the micro-organisms from three soil samples obtained from a subtropical forest of Puerto Iguazú (Argentina), to analyse them for detection of the biotechnologically interesting enzymatic activities lipase, esterase, cellulase, xylanase and pectinase, and to identify the most active strain.A total of 724 strains were isolated using different culture media and temperatures, and 449 of them showed at least one of the hydrolytic activities pursued. Lipolytic activity of the lipid-degrading strains was further determined using MUF-butyrate and MUF-oleate as substrates. The alkalophilic strain CR-179, one of the most active for all the enzymatic activities assayed, was characterized and preliminarily identified by morphological, physiological and 16S rDNA tests, as aBacillussp. closely related toBacillus subtilis.Highly hydrolyticstrains were isolated from all soil samples, suggesting the existence of a microbial community well-adapted to nutrient recycling. Strain CR-179, one of the most active, has been preliminarily identified as aBacillussp.A collection of hydrolytic strains with high biotechnological potential was obtained. Presence of sequences codifying for a lipolytic system related to theB. subtilisgroup lipases was revealed by PCR for the best lipolytic strain. [ABSTRACT FROM AUTHOR]

Abstract Aims: The aim of this study was to perform the isolation, cloning and characterization of a lipase from Bacillus sp. BP-6 bearing the features of a biotechnologically important group of enzymes. Methods and Results: Strain Bacillus sp. BP-6, showing activity on tributyrin plates, was used for isolation of lipase-coding gene lip A by means of inverse and direct PCR. The complete 633 nucleotide ORF isolated was cloned in Escherichia coli for further characterization. The amino acid sequence of the cloned protein was 98% identical to B. subtilis and B. megaterium lipases, the enzyme also showing similar molecular and biochemical features. Conclusions: The gene coding for Bacillus sp. BP-6 LipA was found in all mesophilic Bacillus species assayed, indicating its ubiquity in the genus. The cloned enzyme displayed the same properties as those of homologous lipases. Significance and Impact of the Study: The overall profile of Bacillus sp. BP-6 LipA was found to be that of a ubiquitous and highly conserved subfamily I.4 bacterial lipase. Previously described lipases within this family have shown to be well suited for biotechnological applications, suggesting that the cloned enzyme could be used accordingly. [ABSTRACT FROM AUTHOR]